Results overview: Found 6 records in 0.02 seconds.
Articles, 4 records found
Research literature, 2 records found
Articles 4 records found  
1.
12 p, 1.4 MB Dual-Fluorescent Nanoscale Coordination Polymers via a Mixed-Ligand Synthetic Strategy and Their Use for Multichannel Imaging / Nador, Fabiana (Institut Català de Nanociència i Nanotecnologia) ; Wnuk, Karolina (Institut Català de Nanociència i Nanotecnologia) ; Garcia Pardo, Javier (Institut Català de Nanociència i Nanotecnologia) ; Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Solorzano Rodríguez, Ruben (Institut Català de Nanociència i Nanotecnologia) ; Ruiz Molina, Daniel (Institut Català de Nanociència i Nanotecnologia) ; Novio Vázquez, Fernando (Institut Català de Nanociència i Nanotecnologia)
Two rationally designed strategies for covalent bonding of fluorescent dyes in coordination polymer nanoparticles aiming to achieve bifunctional fluorescent nanostructures have been developed. The first strategy was based on the synthesis of the coordination polymers structured as nanoparticles by coordination of Co ions to two different catechol ligands containing free functional chemical groups (dopamine and 3,4-dihydroxybenzaldehyde), and a bis(imidazole)-based ligand (1,4-bis(imidazole-1-ylmethyl)benzene, bix). [...]
2018 - 10.1002/cnma.201700311
ChemNanoMat, Vol. 4, Issue 2 (February 2018) , p. 183-193  
2.
19 p, 3.2 MB Biochemical and MALDI-TOF mass spectrometric characterization of a novel native and recombinant cystine knot miniprotein from Solanum tuberosum subsp. andigenum cv. Churqueña / Cotabarren, Juliana (Universidad Nacional de La Plata. Centro de Investigación de Proteínas Vegetales (CIPROVE). Departamento de Ciencias Biológicas) ; Tellechea, Mariana Edith (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Tanco, Sebastián Martín (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Lorenzo Rivera, Julia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Garcia Pardo, Javier (Institut Català de Nanociència i Nanotecnologia) ; Avilés, Francesc X. (Francesc Xavier) (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Obregón, Walter David (Universidad Nacional de La Plata. Centro de Investigación de Proteínas Vegetales (CIPROVE). Departamento de Ciencias Biológicas)
Cystine-knot miniproteins (CKMPs) are an intriguing group of cysteine-rich molecules that combine the characteristics of proteins and peptides. Typically, CKMPs are fewer than 50 residues in length and share a characteristic knotted scaffold characterized by the presence of three intramolecular disulfide bonds that form the singular knotted structure. [...]
2018 - 10.3390/ijms19030678
International Journal of Molecular Sciences, Vol. 19, Núm. 3 (February 2018) , art. 678  
3.
9 p, 540.6 KB Biocompatible polydopamine-like particles for the removal of heavy metals at extremely low concentrations / Contreras Rodríguez, Ada Rebeca (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Saiz-Poseu, Javier (Institut Català de Nanociència i Nanotecnologia) ; Garcia Pardo, Javier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Garcia, Beatriz (Institut Català de Nanociència i Nanotecnologia) ; Lorenzo Rivera, Julia (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Ojea-Jiménez, Isaac (Institut Català de Nanociència i Nanotecnologia) ; Komilis, Dimitrios (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química) ; Sedó, Josep (Institut Català de Nanociència i Nanotecnologia) ; Busqué Sánchez, Félix (Universitat Autònoma de Barcelona. Departament de Química) ; Sánchez Ferrer, Antoni (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Ruiz Molina, Daniel (Institut Català de Nanociència i Nanotecnologia) ; Font i Segura, Xavier (Universitat Autònoma de Barcelona. Departament d'Enginyeria Química, Biològica i Ambiental) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular
A family of catechol-based submicron particles, with sizes between 200 and 300 nm, was tested for the removal of Cd(II), Pb(II) and Cr(VI) in water. The highest adsorption capacity was obtained with catecholbased particles in the case of Pb(II), followed by Cd(II). [...]
2016 - 10.1039/c6ra03664c
RSC Advances, Vol. 6 (April 2016) , p. 40058-40066  
4.
11 p, 2.5 MB Synthesis of functionalized fluorescent silver nanoparticles and their toxicological effect in aquatic environments (Goldfish) and HEPG2 cells / Oliveira, Elisabete (Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia) ; Santos, Hugo M. (Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia) ; Garcia Pardo, Javier (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí") ; Diniz, Mário (Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia) ; Lorenzo Rivera, Julia (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Rodríguez-González, Benito (Centro de Apoyo Científico y Tecnológico a la Investigación) ; Capelo, José L. (Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia) ; Lodeiro, Carlos (Universidade Nova de Lisboa. Faculdade de Ciências e Tecnologia)
Silver nanoparticles, AgNPs, are widely used in our daily life, mostly due to their antibacterial, antiviral, and antifungal properties. However, their potential toxicity remains unclear. In order to unravel this issue, emissive AgNPs were first synthetized using an inexpensive photochemical method, and then their permeation was assessed in vivo in goldfish and in vitro in human hepatoma cells (HepG2). [...]
2013 - 10.3389/fchem.2013.00029
Frontiers in chemistry, Vol. 1, art. 29 (Dec. 2013)  

Research literature 2 records found  
1.
267 p, 5.2 MB Caracterización estructural y funcional de dos metalo-carboxipeptidasas de la familia M14 con especifidad de sustrato tipo acídico : carboxipeptidasa citosólica 6 y carboxipeptidasa O humanas / García Guerrero, María del Carmen, autor. ; Avilés, Francesc X., (Francesc Xavier), dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia) ; Lorenzo Rivera, Julia, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Garcia Pardo, Javier, dir. ; Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular.
Las metalo-carboxipeptidasas (MCPs) son exopeptidasas que contienen un átomo de zinc en el centro activo y que participan en la hidrólisis de enlaces peptídicos C-t de péptidos y proteínas. La carboxipeptidasa A1 (CPA1) fue la primera peptidasa M14 identificada y se aisló hace más de 80 años a partir de extractos de páncreas. [...]
Metallo-carboxypeptidases (MCPs) are exopeptidases, which contain a zinc atom in the active site, involved in the hydrolysis of peptide bonds at the C-terminus of peptides and proteins. Carboxypeptidase A1 (CPA1) was the first M14 peptidase identified. [...]

[Barcelona] : Universitat Autònoma de Barcelona, 2017.  
2.
259 p, 7.3 MB Structural and functional characterization of regulatory metallocarboxypeptidases : studies on human carboxypeptidases D and Z, and the transthyretin-like domain / Garcia Pardo, Javier ; Lorenzo Rivera, Julia, dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Avilés, Francesc X., (Francesc Xavier) dir. (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular) ; Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular
Las metalocarboxipeptidasas (MCPs) son enzimas zinc-dependientes que hidrolizan amino ácidos del extremo C terminal en proteínas y péptidos. La primera MCP en ser identificada fue la carboxipeptidasa A1 (CPA1), una enzima pancreática que hidroliza residuos C terminales hidrofóbicos. [...]
Metallocarboxypeptidases (MCPs) are zinc-dependent enzymes that cleave single amino acids from the C termini of proteins and peptides. The first MCP to be identified was carboxypeptidase A1 (CPA1), a pancreatic enzyme that removes C-terminal hydrophobic residues. [...]

Bellaterra : Universitat Autònoma de Barcelona, 2015  

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